Jj. Kim et al., Crystallization and preliminary X-ray diffraction studies of the guanylatekinase-like domain of PSD-95 protein from rat, ACT CRYST D, 57, 2001, pp. 616-617
The PSD-95 (postsynaptic density-95) protein, one of the members of the MAG
UK (membrane-associated guanylate kinase) family, is composed of three PDZ
domains, one SH3 domain and one guanylate kinase-like (GK) domain. The GK d
omain mediates the scaffolding function of PSD-95 by protein-protein intera
ction. Here, the GK domain was subcloned, expressed as an intein fusion pro
tein, purified without the intein and then crystallized at room temperature
by the hanging-drop vapour-diffusion method using PEG 8000 as a precipitan
t. The complete native data set was collected to a resolution of 2.35 Angst
rom using flash-cooling. The crystals belong to the primitive tetragonal sp
ace group P4(3) (or P4(1)), with unit-cell parameters a = b = 70.03 (4), c
= 37.64 (1) Angstrom.